1r4q: Difference between revisions

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-{{Seed}}
-[[Image:1r4q.png|left|200px]]
-<!--
+==Shiga toxin==
-The line below this paragraph, containing "STRUCTURE_1r4q", creates the "Structure Box" on the page.
+<StructureSection load='1r4q' size='340' side='right'caption='[[1r4q]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1r4q]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Shigella_dysenteriae Shigella dysenteriae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R4Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1R4Q FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
--->
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1r4q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r4q OCA], [https://pdbe.org/1r4q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1r4q RCSB], [https://www.ebi.ac.uk/pdbsum/1r4q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1r4q ProSAT]</span></td></tr>
-{{STRUCTURE_1r4q|  PDB=1r4q  |  SCENE=  }}
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/STXA_SHIDY STXA_SHIDY] The A subunit is responsible for inhibiting protein synthesis through the catalytic inactivation of 60S ribosomal subunits. After endocytosis, the A subunit is cleaved by furin in two fragments, A1 and A2: A1 is the catalytically active fragment, and A2 is essential for holotoxin assembly with the B subunits.
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/r4/1r4q_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1r4q ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Several serotypes of Escherichia coli produce protein toxins closely related to Shiga toxin (Stx) from Shigella dysenteriae serotype 1. These Stx-producing E. coli cause outbreaks of hemorrhagic colitis and hemolytic uremic syndrome in humans, with the latter being more likely if the E. coli produce Stx2 than if they only produce Stx1. To investigate the differences among the Stxs, which are all AB(5) toxins, the crystal structure of Stx2 from E. coli O157:H7 was determined at 1.8-A resolution and compared with the known structure of Stx. Our major finding was that, in contrast to Stx, the active site of the A-subunit of Stx2 is accessible in the holotoxin, and a molecule of formic acid and a water molecule mimic the binding of the adenine base of the substrate. Further, the A-subunit adopts a different orientation with respect to the B-subunits in Stx2 than in Stx, due to interactions between the carboxyl termini of the B-subunits and neighboring regions of the A-subunit. Of the three types of receptor-binding sites in the B-pentamer, one has a different conformation in Stx2 than in Stx, and the carboxyl terminus of the A-subunit binds at another. Any of these structural differences might result in different mechanisms of action of the two toxins and the development of hemolytic uremic syndrome upon exposure to Stx2.
-===Shiga toxin===
+Structure of shiga toxin type 2 (Stx2) from Escherichia coli O157:H7.,Fraser ME, Fujinaga M, Cherney MM, Melton-Celsa AR, Twiddy EM, O'Brien AD, James MN J Biol Chem. 2004 Jun 25;279(26):27511-7. Epub 2004 Apr 9. PMID:15075327<ref>PMID:15075327</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1r4q" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_15075327}}, adds the Publication Abstract to the page
+*[[Shiga toxin 3D structures|Shiga toxin 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 15075327 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_15075327}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Large Structures]]
-R4Q is a 12 chains structure of sequences from [http://en.wikipedia.org/wiki/Shigella_dysenteriae Shigella dysenteriae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R4Q OCA].
-==Reference==
-<ref group="xtra">PMID:15075327</ref><references group="xtra"/>
 [[Category: Shigella dysenteriae]]
-[[Category: RRNA N-glycosylase]]
+[[Category: Cherney MM]]
-[[Category: Brien, A D.O.]]
+[[Category: Fraser ME]]
-[[Category: Cherney, M M.]]
+[[Category: Fujinaga M]]
-[[Category: Fraser, M E.]]
+[[Category: James MNG]]
-[[Category: Fujinaga, M.]]
+[[Category: Melton-Celsa AR]]
-[[Category: James, M N.G.]]
+[[Category: O'Brien AD]]
-[[Category: Melton-Celsa, A R.]]
+[[Category: Twiddy EM]]
-[[Category: Twiddy, E M.]]
-[[Category: Ab5 toxin]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 02:24:07 2009''